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Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes.

par Perez-Morga, David ;Vanhollebeke, Benoît ;Hanocq, Françoise ;Nolan, Derek ;Lins, Laurence;Homblé, Fabrice ;Vanhamme, Luc ;Tebabi, Patricia ;Pays Deschutter, Annette ;Poelvoorde, Philippe ;Jacquet, Alain ;Brasseur, Robert ;Pays, Etienne
Référence Science, 309, 5733, page (469-472)
Publication Publié, 2005-07

Article révisé par les pairs

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Résumé :

Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.